Multifaceted roles of HEAT SHOCK PROTEIN 90 molecular chaperones in plant development
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
32293686
DOI
10.1093/jxb/eraa177
PII: 5817050
Knihovny.cz E-zdroje
- Klíčová slova
- Chaperone, HEAT SHOCK PROTEIN 90, client protein, co-chaperone, plant cell, plant development, protein kinase,
- MeSH
- fenotyp MeSH
- genotyp MeSH
- molekulární chaperony genetika MeSH
- proteiny tepelného šoku HSP90 * genetika MeSH
- vývoj rostlin * MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- molekulární chaperony MeSH
- proteiny tepelného šoku HSP90 * MeSH
HEAT SHOCK PROTEINS 90 (HSP90s) are molecular chaperones that mediate correct folding and stability of many client proteins. These chaperones act as master molecular hubs involved in multiple aspects of cellular and developmental signalling in diverse organisms. Moreover, environmental and genetic perturbations affect both HSP90s and their clients, leading to alterations of molecular networks determining respectively plant phenotypes and genotypes and contributing to a broad phenotypic plasticity. Although HSP90 interaction networks affecting the genetic basis of phenotypic variation and diversity have been thoroughly studied in animals, such studies are just starting to emerge in plants. Here, we summarize current knowledge and discuss HSP90 network functions in plant development and cellular homeostasis.
Citace poskytuje Crossref.org
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